| Literature DB >> 10510286 |
T Kishimoto1, M Watanabe, T Mitsui, H Hori.
Abstract
Characterization was done on the sugar chains of glutelin, a major storage protein in rice seeds. The basic subunits of glutelin were shown to be glycoproteins by staining with PAS and the lectins concanavalin A (Con A) and peanut agglutinin (PNA). The binding of PNA to the basic subunits was substantially reduced by treatment of the glutelin with NaIO4, NaOH, or O-glycanase. The sugar chains of the subunits, obtained by hydrazinolysis and O-glycanase, were pyridylaminated and subjected to 2-dimensional HPLC analysis using C(18) and acrylamide-derivatized columns. It was found that the Galbeta-1,3GalNAc disaccharide, which was previously identified as a core 1 structure of mucin-type sugar chains, is conjugated to the glutelin subunits. Furthermore, amino acid sequencing of an 11-kDa peptide of the subunits, recognized by both PNA and Con A, suggested that both N-linked and O-linked glycosylation occurs in the carboxy-terminal region of these subunits. Copyright 1999 Academic Press.Entities:
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Year: 1999 PMID: 10510286 DOI: 10.1006/abbi.1999.1406
Source DB: PubMed Journal: Arch Biochem Biophys ISSN: 0003-9861 Impact factor: 4.013